Copper complexes biomimetic chemistry

The last category was concerned with miscellaneous subjects, while citing some chirogenic porphyrin-based systems. Representative reviews include chiral lanthanide complexes by Aspinall [41], coordination chemistry of tin porphyrins by Arnold and Blok [42], photoprocesses of copper complexes that bind to DNA by McMillin and McNett [43], nonplanar porphyrins and their significance in proteins by Shelnutt et al. [44], cytochrome P450 biomimetic systems by Feiters, Rowan, and Nolte [45] and phthalocyanines by Kobayashi [46,47]. 

Granata, A., Monzani, E., Casella, E. (2004). Mechanistic insight into the catechol oxidase activity by a biomimetic dinuclear copper complex. Journal of Biological Inorganic Chemistry, 9, 189—196. 

Progresses in the study of oxygenations with molecular oxygen partly described above show the expand of chemistry from biomimetic or bioinorganic chemistry to bioinspired catalysis. The use of non-iron and -copper complexes provides not only mechanistic insights into the enzymatic oxygenations as described in Chapters 4 and 6, but different... 

Karlin, K. D. Zuberbuhler, A. D. Formation, structure, and reactivity of copper dioxygen complexes, Bioinorganic Catalysis , 2nd edn. (Revised and Expanded) Eds. Reedijk, J. Bouwman, E. Marcel Dekker New York, 1999, pp. 469-534. Fukuzumi, S. Imahori, H. Biomimetic electron-transfer chemistry of porphyrins and metalloporphyrins, Electron Transfer in Chemistry , Vol. 2 Ed. Balzani, V. Wiley-VCH Verlag GmbH Weinheim, 2001, pp. 927-975. 

This chapter focuses on the chemistry ofbiomimetic copper nitrosyl complexes relevant to the NO-copper interactions in proteins that are central players in dissimilatory nitrogen oxide reduction (denitrification). The current state of knowledge of NO-copper interactions in nitrite reductase, a key denitrifying enzyme, is briefly surveyed the syntheses, structures, and reactivity of copper nitrosyl model complexes prepared to date are presented and the insight these model studies provide into the mechanisms of denitrification and the structures of other copper protein nitrosyl intermediates are discussed. Emphasis is placed on analysis of the geometric features, electronic structures, and biomimetic reactivity with NO or NOf of the only structurally characterized copper nitrosyls, a dicopper(II) complex bridged by NO and a mononuclear tris(pyrazolyl)hydroborate complex having a Cu(I)-NO formulation. 

Biomimetic copper-dioxygen chemistry has advanced considerably since the first structurally-characterized copper-dioxgygen adduct. However, it has been difficult to simulate the room-temperature stability of hemocyanin in these model complexes due to the fact that unlike the enzyme active sites, these models usually do not possess protective environments which can help stabilize potentially reactive copper-dioxygen species. Recently, two room-temperature stable copper-dioxygen complexes have been synthesized which come closer to the goal of mimicking the dioxygen carrier hemocyanin. 

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